ADDITION/CORRECTION pubs.acs.org/JPCB
Correction to “Correlating Aggregation Kinetics and Stationary Diffusion in Protein Sodium Salt Systems Observed with Dynamic Light Scattering” [The Journal of Physical Chemistry B 2010, 114, 4383–4387. DOI: 10.1021/jp912126w]. Jonathan Rubin, Adriana San Miguel, Andreas S. Bommarius,* and Sven H. Behrens The calculation of the coagulation rate constant k11 presented in this paper was performed incorrectly due to a unit conversion error. The corrected plots of Figure 3 differ only in the scale of the ordinates. The corrected values for k11 suggest a new choice of k11 = 10 28 m3/s as the reference rate constant at which to evaluate the ionic strength Is used as a measure of stability in Figure 4. The corrected Is values (Figure 4) are shifted very slightly with respect to the values originally reported, but the corrected data still provide strong support for our original conclusions.
Figure 4. Relating ν and ionic strength at k11 = 10 for lysozyme; (b) correlation for BSA.
28
m3/s: (a) correlation
DOI: 10.1021/jp206633a Published on Web 08/18/2011
Figure 3. Coagulation rate constant, k11, as a function of ionic strength. (a) Lysozyme experiments were run at pH 4.25 and T = 25 °C in a 0.1 M sodium acetate buffer (top). (b) BSA experiments were run at pH 4.0 and T = 25 °C in a 0.1 M sodium acetate buffer (bottom).
The correlation we propose is still robust, as we maintain R2 values of 0.92 or above for both proteins. Characteristic differences between the investigated proteins and the different electrolytes used remain unaffected and our theory and conclusion are still valid. 10778
dx.doi.org/10.1021/jp206633a | J. Phys. Chem. B 2011, 115, 10778–10778
